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Protein

Proteasome subunit beta

Gene

psmB

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.UniRule annotation

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.UniRule annotation

Enzyme regulationi

The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei12 – 121NucleophileUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-494-MONOMER.

Protein family/group databases

MEROPSiT01.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit betaUniRule annotation (EC:3.4.25.1UniRule annotation)
Alternative name(s):
20S proteasome beta subunitUniRule annotation
Proteasome core protein PsmBUniRule annotation
Gene namesi
Name:psmBUniRule annotation
Ordered Locus Names:AF_0481
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
ProteomesiUP000002199 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1111Removed in mature form; by autocatalysisUniRule annotationPRO_0000026659Add
BLAST
Chaini12 – 213202Proteasome subunit betaPRO_0000026660Add
BLAST

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Interactioni

Subunit structurei

The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has probably a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is likely capped at one or both ends by the proteasome regulatory ATPase, PAN.1 Publication

Protein-protein interaction databases

IntActiQ9P996. 1 interaction.
STRINGi224325.AF0481.

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 196Combined sources
Beta strandi22 – 287Combined sources
Beta strandi31 – 333Combined sources
Beta strandi36 – 416Combined sources
Beta strandi45 – 495Combined sources
Beta strandi52 – 587Combined sources
Helixi60 – 8122Combined sources
Helixi87 – 10014Combined sources
Turni101 – 1033Combined sources
Beta strandi108 – 1169Combined sources
Beta strandi119 – 1257Combined sources
Beta strandi131 – 14111Combined sources
Helixi144 – 15411Combined sources
Helixi161 – 17616Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi196 – 1983Combined sources
Helixi200 – 2078Combined sources
Helixi208 – 2103Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2QX-ray2.83H/I/J/K/L/M/N12-213[»]
ProteinModelPortaliQ9P996.
SMRiQ9P996. Positions 12-213.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P996.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0638.
KOiK03433.
OMAiATMGHFI.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_02113_A. Proteasome_B_A.
InterProiIPR029055. Ntn_hydrolases_N.
IPR019983. Pept_T1A_Psome_bsu_arc.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR03634. arc_protsome_B. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9P996-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMIEEKIYK GTTTVGLVCK DGVVMATEKR ATMGNFIASK AAKKIYQIAD
60 70 80 90 100
RMAMTTAGSV GDAQFLARII KIEANLYEIR RERKPTVRAI ATLTSNLLNS
110 120 130 140 150
YRYFPYLVQL LIGGIDSEGK SIYSIDPIGG AIEEKDIVAT GSGSLTAYGV
160 170 180 190 200
LEDRFTPEIG VDEAVELAVR AIYSAMKRDS ASGDGIDVVK ITEDEFYQYS
210
PEEVEQILAK FRK
Length:213
Mass (Da):23,418
Last modified:October 1, 2000 - v1
Checksum:iDA03E480A88F8227
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB90757.1.
PIRiA69310.
RefSeqiNP_069317.1. NC_000917.1.
WP_010877988.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB90757; AAB90757; AF_0481.
GeneIDi1483698.
KEGGiafu:AF0481.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB90757.1.
PIRiA69310.
RefSeqiNP_069317.1. NC_000917.1.
WP_010877988.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2QX-ray2.83H/I/J/K/L/M/N12-213[»]
ProteinModelPortaliQ9P996.
SMRiQ9P996. Positions 12-213.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9P996. 1 interaction.
STRINGi224325.AF0481.

Protein family/group databases

MEROPSiT01.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB90757; AAB90757; AF_0481.
GeneIDi1483698.
KEGGiafu:AF0481.

Phylogenomic databases

eggNOGiCOG0638.
KOiK03433.
OMAiATMGHFI.

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-494-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9P996.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_02113_A. Proteasome_B_A.
InterProiIPR029055. Ntn_hydrolases_N.
IPR019983. Pept_T1A_Psome_bsu_arc.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR03634. arc_protsome_B. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
    Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
    , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
    Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
  2. "Investigations on the maturation and regulation of archaebacterial proteasomes."
    Groll M., Brandstetter H., Bartunik H., Bourenkow G., Huber R.
    J. Mol. Biol. 327:75-83(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS) OF 12-213 IN COMPLEX WITH ALPHA SUBUNIT AND CALPAIN-INHIBITOR I, SUBUNIT.

Entry informationi

Entry nameiPSB_ARCFU
AccessioniPrimary (citable) accession number: Q9P996
Secondary accession number(s): O29769
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.